Evidence map›Paper›PMID 16818232›Full record

ArticleMolecular cell2006

Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65.

E Allen Sickmier, Katherine E Frato, Haihong Shen, Shanthi R Paranawithana, Michael R Green, Clara L Kielkopf

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed
4.3field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

113 citing papers in PubMed, 190 citations in OpenAlex.

  1. Article
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  3. Review
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  7. Clinical case reports · 2025
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  8. Genes · 2025
    Review
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  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Early Splicing Complexes and Human Disease.International journal of molecular sciences · 2023
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

53 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

E Allen SickmierDepartment of Biochemistry and Molecular Biology, Johns Hopkins University Bloomberg School of Public Health, Baltimore, Maryland 21205, USA.
Katherine E Frato
Haihong Shen
Shanthi R Paranawithana
Michael R Green
Clara L Kielkopf
Johns Hopkins University · USHoward Hughes Medical Institute · USUniversity of Massachusetts Chan Medical School · US

Funding

PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
Molecular Recognition During Pre-mRNA SplicingR01GM070503 · NIGMS · UNIVERSITY OF ROCHESTER · PI KIELKOPF, CLARA · 2004 to 2025
$7.9M
SPLICING OF MRNA PRECURSORSR01GM035490 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI GREEN, MICHAEL R · 1985 to 2021
$4.7M
NIGMS NIH HHS GM035490NIGMS NIH HHS GM070503NIGMS NIH HHS R01 GM035490NIGMS NIH HHS R01 GM070503NIGMS NIH HHS T32 GM008403NIGMS NIH HHS T32 GM08403
6 · The paper itself

Abstract

The essential pre-mRNA splicing factor, U2AF(65), guides the early stages of splice site choice by recognizing a polypyrimidine (Py) tract consensus sequence near the 3' splice site. Since Py tracts are relatively poorly conserved in higher eukaryotes, U2AF(65) is faced with the problem of specifying uridine-rich sequences, yet tolerating a variety of nucleotide substitutions found in natural Py tracts. To better understand these apparently contradictory RNA binding characteristics, the X-ray structure of the U2AF(65) RNA binding domain bound to a Py tract composed of seven uridines has been determined at 2.5 A resolution. Specific hydrogen bonds between U2AF(65) and the uracil bases provide an explanation for polyuridine recognition. Flexible side chains and bound water molecules form the majority of the base contacts and potentially could rearrange when the U2AF(65) structure adapts to different Py tract sequences. The energetic importance of conserved residues for Py tract binding is established by analysis of site-directed mutant U2AF(65) proteins using surface plasmon resonance.

Indexed as

Amino Acid SequenceAnimalsCrystallography, X-RayDNAHumansMiceModels, MolecularMolecular Sequence DataNuclear ProteinsPolypyrimidine Tract-Binding ProteinRibonucleoproteinsRNA PrecursorsSequence AlignmentSplicing Factor U2AFUridineDNANuclear ProteinsPolypyrimidine Tract-Binding ProteinRibonucleoproteinsRNA PrecursorsSplicing Factor U2AFU2AF2 protein, humanUridineZrsr1 protein, mouse

Identifiers

PMID16818232
PMCPMC2043114
OpenAlexW2109618665

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.